Sec-independent translocation of a 100-residue periplasmic N-terminal tail in the E. coli inner membrane protein proW.

@article{Whitley1994SecindependentTO,
  title={Sec-independent translocation of a 100-residue periplasmic N-terminal tail in the E. coli inner membrane protein proW.},
  author={Penn P. Whitley and Thomas Zander and Michael Ehrmann and Martin Haardt and Erhard Bremer and Gunnar von Heijne},
  journal={The EMBO journal},
  year={1994},
  volume={13 19},
  pages={4653-61}
}
The ProW protein, located in the inner membrane of Escherichia coli, has a very unusual topology with a 100-residue-long N-terminal tail protruding into the periplasmic space. We have studied the mechanism of membrane translocation of the periplasmic tail by analysing ProW-PhoA and ProW-Lep fusion proteins, both in wild-type cells and in cells with an impaired sec machinery. Our results show that the translocation efficiency is not affected by treatments that compromise the SecA and SecY… CONTINUE READING